RNA-binding domain proteins in kinetoplastids: A comparative analysis
RNA-binding domain proteins in kinetoplastids: A comparative analysis
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DOI：
10.1128/ec.4.12.2106-2114.2005
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发表时间：
2005-12-01
期刊：
影响因子：
--
通讯作者：
Clayton, C
中科院分区：
文献类型：
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作者：
De Gaudenzi, J;Frasch, AC;Clayton, C
RNA结合蛋白在RNA加工、功能和破坏的许多方面都很重要。一类这样的蛋白质含有RNA识别基序（RRM），其由约90个氨基酸残基组成，包括典型的RNP 1八肽：（K/R）G（F/Y）（G/A）FVX（F/Y）。我们使用了各种同源性搜索，分类所有的RRM蛋白的三个动质体布氏锥虫，克氏锥虫，利什曼原虫主要。所有这三种生物都有类似的含RRM蛋白质直系同源物，这表明共同的转录后加工和调控途径。在T. brucei，只有13个在其他真核生物中有明确的同源物，尽管另外8个可以被赋予推定的功能分配。与专性细胞内寄生虫兔脑炎原虫的18个RRM蛋白质的比较显示，只有3个RRM蛋白质似乎在整个真核生物进化过程中在一级序列水平上是保守的：poly（A）结合蛋白，rRNA加工蛋白MRD 1和核帽结合蛋白。
RNA-binding proteins are important in many aspects of RNA processing, function, and destruction. One class of such proteins contains the RNA recognition motif (RRM), which consists of about 90 amino acid residues, including the canonical RNP1 octapeptide: (K/R)G(F/Y)(G/A)FVX(F/Y). We used a variety of homology searches to classify all of the RRM proteins of the three kinetoplastids Trypanosoma brucei, Trypanosoma cruzi, and Leishmania major. All three organisms have similar sets of RRM-containing protein orthologues, suggesting common posttranscriptional processing and regulatory pathways. Of the 75 RRM proteins identified in T. brucei, only 13 had clear homologues in other eukaryotes, although 8 more could be given putative functional assignments. A comparison with the 18 RRM proteins of the obligate intracellular parasite Encephalitozoon cuniculi revealed just 3 RRM proteins which appear to be conserved at the primary sequence level throughout eukaryotic evolution: poly(A) binding protein, the rRNA-processing protein MRD1, and the nuclear cap binding protein.